712-30-1

Basic information

• Product Name: 2-AMINO-4-HYDROXY-PTERIDINE-6-CARBALDEHYDE
• Synonyms: 2-AMINO-4-HYDROXY-PTERIDINE-6-CARBALDEHYDE;2-amino-4-hydroxy-6-formylpteridine;2-Amino-1,4-dihydro-4-oxopteridine-6-carbaldehyde;2-Amino-3,4-dihydro-4-oxo-6-pteridinecarbaldehyde;2-Amino-4-oxo-1,4-dihydropteridine-6-carbaldehyde;2-Amino-6-formylpteridine-4(3H)-one;6-Formylpterin;Pterine-6-aldehyde
• CAS NO: 712-30-1
• Molecular Formula: C₇H₅N₅O₂
• Molecular Weight: 191.1469
• Product Categories: Heterocycles;Intermediates & Fine Chemicals;Pharmaceuticals
• Mol File: 712-30-1.mol
• Article Data: 23

Chemical Properties

• Melting Point: 280 °C (decomp)
• Boiling Point: 489.1 °C at 760 mmHg
• Flash Point: 249.6 °C
• Appearance: /
• Density: 1.94 g/cm³
• Vapor Pressure: 1.03E-09mmHg at 25°C
• Refractive Index: 1.892
• PKA: pKa 2.0(H2O,t undefined,I=0.1) (Uncertain)
• CAS DataBase Reference: 2-AMINO-4-HYDROXY-PTERIDINE-6-CARBALDEHYDE(CAS DataBase Reference)
• NIST Chemistry Reference: 2-AMINO-4-HYDROXY-PTERIDINE-6-CARBALDEHYDE(712-30-1)
• EPA Substance Registry System: 2-AMINO-4-HYDROXY-PTERIDINE-6-CARBALDEHYDE(712-30-1)

Safety Data

• Hazardous Substances Data: 712-30-1(Hazardous Substances Data)

Usage

Chemical Properties

Yellow Solid

Uses

pteridine derivative, may act as an inhibitor to enzymes involved in ROS management

Definition

ChEBI: Pterin carrying a formyl group at position 6.

InChI:InChI=1/C7H5N5O2/c8-7-11-5-4(6(14)12-7)10-3(2-13)1-9-5/h1-2H,(H3,8,9,11,12,14)

Upstream product

• 735-67-1 2-amino-6-(1,2,3,4-tetrahydroxybutyl)-3H-pteridin-4-one 
• 19962-30-2 N-(6-methyl-4-oxo-1,4-dihydropteridin-2-yl)acetamide 
• 29769-49-1 2-acetylamino-4-hydroxy-6-formylpteridine 
• 117267-22-8 2-Pivaloylamino-6-formylpteridin-4-one 
• 59453-01-9 2-amino-4-hydroxy-6-formylpteridine dimethyl acetal 
• 712-29-8 2-amino-4-hydroxy-6-hydroxymethylpteridine 
• 59-30-3 folic acid 
• 108473-08-1 N-(6-chloro-4-oxo-3,4-dihydropteridin-2-yl)-2,2-dimethylpropanamide 
• 22150-76-1 L-erythro biopterin 
• 65434-55-1 6-formyl-5,8-dihydropterin 
• 6779-87-9 7,8-dihydro-L-biopterin 
• 13214-44-3 6-formyl-7,8-dihydropterin 
• 59-30-3 folate 
• 59-30-3 2-{4-[(2-amino-4-hydroxy-pteridin-6-ylmethyl)-amino]-benzoylamino}-pentanedioic acid 

Downstream Products

• 29769-49-1 N(2')-acetyl-6-formylpterin 
• 189629-53-6 2-(N,N-dimethylaminomethyleneamino)-6-formylpteridin-4(3H)-one 
• 117267-22-8 2-Pivaloylamino-6-formylpteridin-4-one 
• 712-29-8 6-(hydroxymethyl)pterin 
• 171777-72-3 <2',3',5',6'-2H4>folic acid 
• 171777-71-2 N(2')-acetyl-6-benzoyl)-L-glutamic acid diethyl ester>-pterin 
• 171777-70-1 N(2')-acetyl-6-benzoyl)-L-glutamic acid diethyl ester-azomethin>-pterin 
• 948-60-7 pterine-6-carboxylic acid 
• 2236-60-4 2-aminopteridin-4(3H)-one 

Relevant articles and documents

Generation of Reactive Oxygen Species during the Photolysis of 6-(Hydroxymethyl)pterin in Alkaline Aqueous Solutions

Photochemical studies of the reactivity of 6-(hydroxymethyl)pterin (=2-amino-6-(hydroxymethyl)pteridin-4(1H)-one; HPT) in alkaline aqueous solutions (pH 10.2-10.8) at 350 nm and room temperature were performed. The photochemical reactions were followed by UV/VIS spectrophotometry, thin-layer chromatography (TLC), high-performance liquid chromatography (HPLC), and an enzymatic method for H2O2 determination. In the presence of O2, 6-formylpterin (=2-amino-3,4-dihydro-4-oxopteridine-6-carboxaldehyde; FPT) was the only photoproduct detected. In the absence of O2, we observed a compound with an absorbance maximum at 480 nm, which was oxidized very rapidly by O 2 in a dark reaction to yield FPT. The quantum yields of substrates disappearance and of photoproducts formation were determined. The formation of H2O2 during photooxidation was monitored, and the number of mol of H2O2 released per mol of HPT consumed corresponded to a 1: 1 stoichiometry. HPT was also investigated for efficiency of singlet-oxygen (1O2) production and quenching in aqueous solution. The quantum yield of 1O2 production (ΦΔ = 0.21 ± 0.01) was determined by measurements of the 1O2 luminescence in the near-IR (1270 nm) upon continuous excitation of the sensitizer. The rate constant of 1O 2 total quenching by HPT was determined (kt = 3.1 · 106 M-1 s-1), indicating that this compound was able to quench 1O2. However, 1O2 did not participate in the photooxidation of HPT to FPT.

Visible-light photochemistry of 6-formyl-7,8-dihydropterin in aqueous solution

Pterins are a family of heterocyclic compounds present in a wide range of living systems and are involved in different photobiological processes. 6-Formyl-7,8-dihydropterin (H2Fop), is a product of oxidation of several natural occurring pterin derivatives, and its absorption spectrum presents as special feature an intense band in the visible region. Studies of the photochemistry of H2Fop in aqueous solutions under visible radiation and room temperature were performed. The photochemical reactions were followed by UV-vis spectrophotometry, electrochemical measurement of dissolved O2, enzymatic methods for H2O2 determination and HPLC. When H2Fop in air-equilibrated solution was exposed to light, O2 was consumed, the reactant was oxidized to 6-formylpterin (Fop), and H2O2 released. When the photolysis took place in the absence of O2, a red compound was generated. This product was rapidly oxidized to Fop on admission of O2. The quantum yields of H2Fop disappearance and of photoproducts formation are reported and the effect of pH is analyzed. The potential biological implications of the results obtained are also discussed.

Isolation of L-monopterin from Pseudomonas roseum fluorescens J.C. Marchal 1937 and its constitution clarification

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Effect of pterin impurities on the fluorescence and photochemistry of commercial folic acid

Folic acid, or pteroyl?L?glutamic acid (PteGlu) is a conjugated pterin derivative that is used in dietary supplementation as a source of folates, a group of compounds essential for a variety of physiological functions in humans. Photochemistry of PteGlu is important because folates are not synthesized by mammals, undergo photodegradation and their deficiency is related to many diseases. We have demonstrated that usual commercial PteGlu is unpurified with the unconjugated oxidized pterins 6?formylpterin (Fop) and 6?carboxypterin (Cap). These compounds are in such low amounts that a normal chromatographic control would not detect any pterinic contamination. However, the fluorescence of PteGlu solutions is due to the emission of Fop and Cap and the contribution of the PteGlu emission, much lower, is negligible. This is because the fluorescence quantum yield (ΦF) of PteGlu is extremely weak compared to the ΦF of Fop and Cap. Likewise, the PteGlu photodegradation upon UV-A radiation is an oxidation photosensitized by oxidized unconjugated pterins present in the solution, and not a process initiated by the direct absorption of photons by PteGlu. In brief, the fluorescence and photochemical properties of PteGlu solutions, prepared using commercially available solids, are due to their unconjugated pterins impurities and not to PteGlu itself. This fact calls into question many reported studies on fluorescence and photooxidation of this compound.

Photoinactivation of tyrosinase sensitized by folic acid photoproducts

Tyrosinase catalyzes in mammals the first and rate-limiting step in the biosynthesis of the melanin, the main pigment of the skin. Pterins, heterocyclic compounds able to photoinduce oxidation of biomolecules, accumulate in the skin of patients suffering from vitiligo, where there is a lack of melanin. Folic acid (PteGlu) is a conjugated pterin widespread in biological systems. Aqueous solutions of tyrosinase were exposed to UV-A irradiation (350 nm) in the presence of PteGlu and its photoproducts (6-formylpterin and 6-carboxypterin). The reactions were followed by UV-Vis spectrophotometry, enzyme activity measurement, fluorescence spectroscopy and HPLC. In this work, we present data that demonstrate unequivocally that solutions of tyrosinase exposed to UV-A irradiation in the presence of PteGlu, undergo enzyme inactivation. However, PteGlu itself causes a negligible effect on the activity of the enzyme. In contrast, PteGlu photoproducts are efficient photosensitizers. The tyrosinase inactivation involves two different pathways: (i) a photosensitization process and (ii) the oxidation of the enzyme by the hydrogen peroxide produced during the photooxidation of PteGlu and its photoproduct. The former pathway affects both the active site and the tryptophan residues, whereas the latter affects only the active site. The biological implications of the results are discussed.